ID A0A1F2P985_9EURY Unreviewed; 395 AA.
AC A0A1F2P985;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=[Ni-Fe]-hydrogenase large subunit {ECO:0000313|EMBL:OFV67552.1};
GN ORFNames=SCAL_001470 {ECO:0000313|EMBL:OFV67552.1};
OS Candidatus Syntrophoarchaeum caldarius.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster;
OC Syntrophoarchaeum.
OX NCBI_TaxID=1838285 {ECO:0000313|EMBL:OFV67552.1, ECO:0000313|Proteomes:UP000186940};
RN [1] {ECO:0000313|EMBL:OFV67552.1, ECO:0000313|Proteomes:UP000186940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BOX2 {ECO:0000313|EMBL:OFV67552.1};
RA Laso-Perez R., Richter M., Wegener G., Musat F.;
RT "Microbial consortia oxidize butane by reversing methanogenesis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC family. {ECO:0000256|ARBA:ARBA00006605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFV67552.1}.
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DR EMBL; LYOS01000004; OFV67552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2P985; -.
DR STRING; 1838285.SCAL_001470; -.
DR PATRIC; fig|1838285.3.peg.1493; -.
DR Proteomes; UP000186940; Unassembled WGS sequence.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 4.10.480.10; Cytochrome-c3 hydrogenase, C-terminal domain; 1.
DR Gene3D; 3.40.50.700; NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 1.
DR InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR037148; NiFe-Hase_small_C_sf.
DR InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR NCBIfam; TIGR00391; hydA; 1.
DR PANTHER; PTHR30013:SF7; HYDROGENASE-2 SMALL CHAIN; 1.
DR PANTHER; PTHR30013; NIFE / NIFESE HYDROGENASE SMALL SUBUNIT FAMILY MEMBER; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR PRINTS; PR00614; NIHGNASESMLL.
DR SUPFAM; SSF56770; HydA/Nqo6-like; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|PIRSR:PIRSR000310-1};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000310-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000310-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000310-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000310-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000186940};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 66..239
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
FT DOMAIN 260..334
FT /note="Cytochrome-c3 hydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14720"
FT REGION 337..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 284
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 299
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 318
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
FT BINDING 321
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000310-1"
SQ SEQUENCE 395 AA; 42285 MW; 142885EECCF12D50 CRC64;
MKDLKLTKIE DLRNIDILNL DRRTFLKVVG AVGASIFLGT YKTEIVRGLM ESSTSTNLIW
LEGQDCAGCT ISFLNAEQPD VIQAIMDLNV VPQYWETVMI QQGLFVDGVP VENADLNANY
ALELIKESEK DFVLVVEGAI PRGPDGTGNF CRVGGEPFKK IIEDLAPHSL ATVAVGSCAS
YGGIPAGDPN PSDCSGLQFY RKEKGGILGE NYRSKAGLPV INLPCCPTHP DWVMSTLAAV
ILGKTGDIEL DEYNRPTAFF GESIHETCPR RGYYEALKFG MEYCLYGLGC KGPFTSAECP
LRLWNNGRNM CTQAGAPCIG CAEPDFPDGK SPFYLPSGAT ATSSVEKPTA TPVTPTATPT
GTPTATEEVA PGFGAAAAVG AGTLAAARYL KDRRE
//
